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Protein

Vesicle-fusing ATPase

Gene

Nsf

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required for vesicle-mediated transport. Catalyzes the fusion of transport vesicles within the Golgi cisternae. Is also required for transport from the endoplasmic reticulum to the Golgi stack. Seems to function as a fusion protein required for the delivery of cargo proteins to all compartments of the Golgi stack GRIA2 leads to influence GRIA2 membrane cycling (By similarity).By similarity

Catalytic activityi

ATP + H2O = ADP + phosphate.

Cofactori

Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi550 – 5501Magnesium

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi505 – 5106ATPBy similarity
Nucleotide bindingi545 – 5528ATPBy similarity

GO - Molecular functioni

  1. ATPase activity, coupled Source: MGI
  2. ATP binding Source: UniProtKB-KW
  3. metal ion binding Source: UniProtKB-KW
  4. PDZ domain binding Source: MGI
  5. protein complex binding Source: MGI
  6. protein kinase binding Source: ParkinsonsUK-UCL
  7. syntaxin-1 binding Source: ParkinsonsUK-UCL
  8. syntaxin binding Source: MGI

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. Golgi to plasma membrane protein transport Source: GO_Central
  3. Golgi vesicle docking Source: GO_Central
  4. intra-Golgi vesicle-mediated transport Source: GO_Central
  5. positive regulation of receptor recycling Source: MGI
  6. potassium ion transport Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_253367. Trafficking of GluR2-containing AMPA receptors.

Names & Taxonomyi

Protein namesi
Recommended name:
Vesicle-fusing ATPase (EC:3.6.4.6)
Alternative name(s):
N-ethylmaleimide-sensitive fusion protein
Short name:
NEM-sensitive fusion protein
Suppressor of K(+) transport growth defect 2
Short name:
Protein SKD2
Vesicular-fusion protein NSF
Gene namesi
Name:Nsf
Synonyms:Skd2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:104560. Nsf.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. extracellular vesicular exosome Source: MGI
  3. Golgi stack Source: GO_Central
  4. lysosomal membrane Source: MGI
  5. myelin sheath Source: UniProtKB
  6. plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi569 – 5691S → A: Abolishes phosphorylation by CDK16. 1 Publication
Mutagenesisi569 – 5691S → E: Interferes with oligomerization. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 744744Vesicle-fusing ATPasePRO_0000084564Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei105 – 1051N6-acetyllysine1 Publication
Modified residuei259 – 2591Phosphotyrosine1 Publication
Modified residuei569 – 5691Phosphoserine; by CDK161 Publication

Post-translational modificationi

Phosphorylation at Ser-569 interferes with homohexamerization.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP46460.
PaxDbiP46460.
PRIDEiP46460.

2D gel databases

REPRODUCTION-2DPAGEP46460.

PTM databases

PhosphoSiteiP46460.

Expressioni

Gene expression databases

BgeeiP46460.
CleanExiMM_NSF.
ExpressionAtlasiP46460. baseline and differential.
GenevestigatoriP46460.

Interactioni

Subunit structurei

Homohexamer. Interacts with GABARAP and GABARAPL2. Interacts with GRIA2. Interacts with PLK2, leading to disrupt the interaction with GRIA2. Interacts with MUSK; may regulate MUSK endocytosis and activity (By similarity). Interacts with CDK16.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Dlg4Q621084EBI-398006,EBI-300895
Lrrk2Q5S0063EBI-398006,EBI-2693710
MuskQ61006-35EBI-398006,EBI-6308424
Ptpn9O352393EBI-398006,EBI-7297868

Protein-protein interaction databases

BioGridi201857. 5 interactions.
IntActiP46460. 19 interactions.
MINTiMINT-89339.

Structurei

3D structure databases

ProteinModelPortaliP46460.
SMRiP46460. Positions 1-201, 220-742.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AAA ATPase family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0464.
GeneTreeiENSGT00530000064085.
HOVERGENiHBG000324.
InParanoidiP46460.
KOiK06027.
OMAiFKDKERS.
OrthoDBiEOG7P8P7F.
PhylomeDBiP46460.
TreeFamiTF300371.

Family and domain databases

Gene3Di3.10.330.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR003593. AAA+_ATPase.
IPR009010. Asp_de-COase-like_dom.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR004201. Cdc48_dom2.
IPR029067. CDC48_domain_2-like.
IPR003338. CDC4_N-term_subdom.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00004. AAA. 2 hits.
PF02933. CDC48_2. 1 hit.
PF02359. CDC48_N. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 2 hits.
SM01072. CDC48_2. 1 hit.
SM01073. CDC48_N. 1 hit.
[Graphical view]
SUPFAMiSSF50692. SSF50692. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF54585. SSF54585. 1 hit.
PROSITEiPS00674. AAA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P46460-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAGRTMQAAR CPTDELSLSN CAVVNEKDFQ SGQHVMVRTS PNHKYIFTLR
60 70 80 90 100
THPSVVPGCI AFSLPQRKWA GLSIGQDIEV ALYSFDKAKQ CIGTMTIEID
110 120 130 140 150
FLQKKNIDSN PYDTDKMAAE FIQQFNNQAF SVGQQLVFSF NDKLFGLLVK
160 170 180 190 200
DIEAMDPSIL KGEPASGKRQ KIEVGLVVGN SQVAFEKAEN SSLNLIGKAK
210 220 230 240 250
TKENRQSIIN PDWNFEKMGI GGLDKEFSDI FRRAFASRVF PPEIVEQMGC
260 270 280 290 300
KHVKGILLYG PPGCGKTLLA RQIGKMLNAR EPKVVNGPEI LNKYVGESEA
310 320 330 340 350
NIRKLFADAE EEQRRLGANS GLHIIIFDEI DAICKQRGSM AGSTGVHDTV
360 370 380 390 400
VNQLLSKIDG VEQLNNILVI GMTNRPDLID EALLRPGRLE VKMEIGLPDE
410 420 430 440 450
KGRLQILHIH TARMRGHQLL SADVDIKELA VETKNFSGAE LEGLVRAAQS
460 470 480 490 500
TAMNRHIKAS TKVEVDMEKA ESLQVTRGDF LASLENDIKP AFGTNQEDYA
510 520 530 540 550
SYIMNGIIKW GDPVTRVLDD GELLVQQTKN SDRTPLVSVL LEGPPHSGKT
560 570 580 590 600
ALAAKIAEES NFPFIKICSP DKMIGFSETA KCQAMKKIFD DAYKSQLSCV
610 620 630 640 650
VVDDIERLLD YVPIGPRFSN LVLQALLVLL KKAPPQGRKL LIIGTTSRKD
660 670 680 690 700
VLQEMEMLNA FSTTIHVPNI ATGEQLLEAL ELLGNFKDKE RTTIAQQVKG
710 720 730 740
KKVWIGIKKL LMLIEMSLQM DPEYRVRKFL ALMREEGASP LDFD
Length:744
Mass (Da):82,613
Last modified:May 1, 2007 - v2
Checksum:iBE55AD0056AD5585
GO

Sequence cautioni

The sequence CAM20943.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAM23742.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti300 – 3001A → G in BAC39361. (PubMed:16141072)Curated
Sequence conflicti316 – 32611LGANSGLHIII → VCGHKTNLLKM in BAC34637. (PubMed:16141072)CuratedAdd
BLAST
Sequence conflicti492 – 4921F → I in AAA50498. (PubMed:8082782)Curated
Sequence conflicti552 – 5521L → V in AAA50498. (PubMed:8082782)Curated
Sequence conflicti657 – 6571M → I in BAC25937. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U10120 mRNA. Translation: AAA50498.1.
AK028415 mRNA. Translation: BAC25937.1.
AK032120 mRNA. Translation: BAC27713.1.
AK049281 mRNA. Translation: BAC33656.1.
AK051430 mRNA. Translation: BAC34637.1.
AK085086 mRNA. Translation: BAC39361.1.
AK153905 mRNA. Translation: BAE32247.1.
AL596108, AL603829 Genomic DNA. Translation: CAM20943.1. Sequence problems.
AL596108, AL603829 Genomic DNA. Translation: CAM20945.1.
AL603829, AL596108 Genomic DNA. Translation: CAM23742.1. Sequence problems.
AL603829, AL596108 Genomic DNA. Translation: CAM23743.1.
BC006627 mRNA. Translation: AAH06627.1.
BC019167 mRNA. Translation: AAH19167.1.
CCDSiCCDS25524.1.
RefSeqiNP_032766.2. NM_008740.4.
UniGeneiMm.260117.
Mm.474887.

Genome annotation databases

EnsembliENSMUST00000103075; ENSMUSP00000099364; ENSMUSG00000034187.
GeneIDi18195.
KEGGimmu:18195.
UCSCiuc007lvt.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U10120 mRNA. Translation: AAA50498.1.
AK028415 mRNA. Translation: BAC25937.1.
AK032120 mRNA. Translation: BAC27713.1.
AK049281 mRNA. Translation: BAC33656.1.
AK051430 mRNA. Translation: BAC34637.1.
AK085086 mRNA. Translation: BAC39361.1.
AK153905 mRNA. Translation: BAE32247.1.
AL596108, AL603829 Genomic DNA. Translation: CAM20943.1. Sequence problems.
AL596108, AL603829 Genomic DNA. Translation: CAM20945.1.
AL603829, AL596108 Genomic DNA. Translation: CAM23742.1. Sequence problems.
AL603829, AL596108 Genomic DNA. Translation: CAM23743.1.
BC006627 mRNA. Translation: AAH06627.1.
BC019167 mRNA. Translation: AAH19167.1.
CCDSiCCDS25524.1.
RefSeqiNP_032766.2. NM_008740.4.
UniGeneiMm.260117.
Mm.474887.

3D structure databases

ProteinModelPortaliP46460.
SMRiP46460. Positions 1-201, 220-742.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201857. 5 interactions.
IntActiP46460. 19 interactions.
MINTiMINT-89339.

PTM databases

PhosphoSiteiP46460.

2D gel databases

REPRODUCTION-2DPAGEP46460.

Proteomic databases

MaxQBiP46460.
PaxDbiP46460.
PRIDEiP46460.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000103075; ENSMUSP00000099364; ENSMUSG00000034187.
GeneIDi18195.
KEGGimmu:18195.
UCSCiuc007lvt.1. mouse.

Organism-specific databases

CTDi4905.
MGIiMGI:104560. Nsf.

Phylogenomic databases

eggNOGiCOG0464.
GeneTreeiENSGT00530000064085.
HOVERGENiHBG000324.
InParanoidiP46460.
KOiK06027.
OMAiFKDKERS.
OrthoDBiEOG7P8P7F.
PhylomeDBiP46460.
TreeFamiTF300371.

Enzyme and pathway databases

ReactomeiREACT_253367. Trafficking of GluR2-containing AMPA receptors.

Miscellaneous databases

ChiTaRSiNsf. mouse.
NextBioi293548.
PROiP46460.
SOURCEiSearch...

Gene expression databases

BgeeiP46460.
CleanExiMM_NSF.
ExpressionAtlasiP46460. baseline and differential.
GenevestigatoriP46460.

Family and domain databases

Gene3Di3.10.330.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR003593. AAA+_ATPase.
IPR009010. Asp_de-COase-like_dom.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR004201. Cdc48_dom2.
IPR029067. CDC48_domain_2-like.
IPR003338. CDC4_N-term_subdom.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00004. AAA. 2 hits.
PF02933. CDC48_2. 1 hit.
PF02359. CDC48_N. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 2 hits.
SM01072. CDC48_2. 1 hit.
SM01073. CDC48_N. 1 hit.
[Graphical view]
SUPFAMiSSF50692. SSF50692. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF54585. SSF54585. 1 hit.
PROSITEiPS00674. AAA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a novel mammalian member of the NSF/CDC48p/Pas1p/TBP-1 family through heterologous expression in yeast."
    Perier F., Coulter K.L., Liang H., Radeke C.M., Gaber R.F., Vandenberg C.A.
    FEBS Lett. 351:286-290(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Head, Lung, Medulla oblongata, Spinal ganglion and Thymus.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Eye and Mammary tumor.
  5. Lubec G., Kang S.U., Klug S., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 45-50; 69-87; 106-116; 151-161; 170-198; 218-232; 255-266; 294-303; 305-314; 316-335; 338-357; 404-413; 416-427; 435-446; 517-529; 534-559; 573-581; 595-631; 640-648 AND 710-725, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6 and OF1.
    Tissue: Brain and Hippocampus.
  6. "Pctaire1 phosphorylates N-ethylmaleimide-sensitive fusion protein: implications in the regulation of its hexamerization and exocytosis."
    Liu Y., Cheng K., Gong K., Fu A.K., Ip N.Y.
    J. Biol. Chem. 281:9852-9858(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CDK16, SUBUNIT, MUTAGENESIS OF SER-569, PHOSPHORYLATION AT SER-569.
  7. "Muscle-specific receptor tyrosine kinase endocytosis in acetylcholine receptor clustering in response to agrin."
    Zhu D., Yang Z., Luo Z., Luo S., Xiong W.C., Mei L.
    J. Neurosci. 28:1688-1696(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MUSK.
  8. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
    Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
    J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-259, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  9. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiNSF_MOUSE
AccessioniPrimary (citable) accession number: P46460
Secondary accession number(s): A2A646
, Q8BQ65, Q8C3R2, Q8CCT9, Q8CEF0, Q923C6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: May 1, 2007
Last modified: February 4, 2015
This is version 140 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.